期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 56, 期 20, 页码 5490-5493出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201700411
关键词
Bell's model; catch bonds; protein unfolding; titin; transition states
资金
- Fundamental Research Funds for the Central Universities [2013121005]
- National Nature Science Foundation of China [11474237, 11574310]
- 111 Project [B16029]
- National Research Foundation of Singapore through Mechanobiology Institute
- National Research Foundation (NRF), Prime Minister's Office, Singapore under its NRF Investigatorship Programme (NRF Investigatorship Award) [NRF-NRFI2016-03]
The giant protein titin plays a critical role in regulating the passive elasticity of muscles, mainly through the stochastic unfolding and refolding of its numerous immunoglobulin domains in the I-band of sarcomeres. The unfolding dynamics of titin immunoglobulin domains at a force range greater than 100 pN has been studied by atomic force microscopy, while that at smaller physiological forces has not been measured before. By using magnetic tweezers, it is found that the titin I27 domain unfolds in a surprising non-monotonic force-dependent manner at forces smaller than 100 pN, with the slowest unfolding rate occurring around 22 pN. We further demonstrate that a model with single unfolding pathway taking into account the elasticity of the transition state can reproduce the experimental results. These results provide important novel insights into the regulation mechanism of the passive elasticity of muscle tissues.
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